Biophysical and flavonoid-binding studies of the G protein ectodomain of group A human respiratory syncytial virus

Heliyon

Fátima Pereira de Souza¹  Karina Alves de Toledo¹  Jéssica Maróstica de Sá²  Ícaro Putinhon Caruso³  Vitor Brassolatti Machado⁴  Marcelo Andres Fossey⁵  Ana Karla Miranda Prado⁶  Luis Octávio Regasini⁶ 

[1] Instituto de Biociências, Letras e Ciências Exatas, UNESP, Department of Physics, São José do Rio Preto, SP, Brazil;Instituto de Biociências, Letras e Ciências Exatas, UNESP, Multiuser Center for Biomolecular Innovation, Laboratory of Molecular Biology, São José do Rio Preto, SP, Brazil;Faculdade de Ciências e Letras, UNESP, Department of Biology Sciences, Assis, SP, Brazil;Instituto de Biociências, Letras e Ciências Exatas, UNESP, Department of Biology, São José do Rio Preto, SP, Brazil;Instituto de Biociências, Letras e Ciências Exatas, UNESP, Department of Chemistry and Environmental Sciences, São José do Rio Preto, SP, Brazil;Instituto de Biociências, Letras e Ciências Exatas, UNESP, Multiuser Center for Biomolecular Innovation, Laboratory of Molecular Biology, São José do Rio Preto, SP, Brazil;

关键词: Biochemistry;    Biophysics;    Molecular biology;   

DOI  :  

来源: DOAJ

【 摘 要 】

The human Respiratory Syncytial Virus (hRSV) is the major causative agent of lower respiratory tract diseases in infants, young children and elderly. The membrane protein G is embedded in the viral lipid envelope and plays an adhesion function of the virus to host cells. The present study reports the production of the group A hRSV recombinant G protein ectodomain (edG) and its characterization of secondary structure and thermal unfolding by circular dichroism (CD), as well as the binding investigation of flavonoids quercetin and morin to this protein by fluorescent quenching. CD data reveal that edG is composed mostly of β-structure and its melting temperature is of 325 K. Fluorescence quenching experiments of hRSV edG show that the dissociation constants for the flavonoids binding are micromolar and the binding affinity for the edG/quercetin complex is inversely dependent on rising temperature while is directly dependent for the edG/morin interaction. The thermodynamic parameters suggest that hydrophobic contacts are important for the edG/morin association while van der Waals forces and hydrogen bonds contribute to the stabilization of the edG/quercetin complex. Thus, data reported herein may contribute to the development of new treatment strategies that prevent the viral infection by hRSV.

【 授权许可】

Unknown